ライフサイエンスコーパス: MARCKS

1 MARCKS (myristoylated alanine-rich C-kinase substrate) i

2 MARCKS acted upstream of the AKT/mTOR pathway, activatin

3 MARCKS associates with membranes via the combined action

4 MARCKS binds with its functionally essential effector do

5 MARCKS expression and signaling in primary MKs is a nove

6 MARCKS inhibition by peptide significantly decreased pro

7 MARCKS is a protein kinase C (PKC) substrate that binds

8 MARCKS is an actin-binding protein that modulates vascul

9 MARCKS is known to be phosphorylated by Cdk5 in chick ne

10 MARCKS is required for neural tube closure, but the regu

11 MARCKS knockdown and H(2)O(2) treatment alter the archit

12 MARCKS phosphorylation has been implicated in endocytosi

13 MARCKS phosphorylation was inhibited by PKC-delta siRNA,

14 MARCKS supports development, synaptic plasticity, and re

15 MARCKS-deficient mouse embryonic fibroblasts (MEFs) resp

16 MARCKS-ED has the added property of being a lower-molecu

17 MARCKS-like protein (MLP), recently discovered as a rege

18 ion of wild-type and PSD-mutated (S159/163A) MARCKS, we showed that elevated phospho-MARCKS promoted

19 DARPP-32 binds to adducin MARCKS domain and this interaction is modulated by DARPP

20 S or EGFR mutations, and establishes an AKT1-MARCKS-LAMC2 feedback loop in this regulation.

21 subsequent loss of activation of GAP-43 and MARCKS, and the established role of PKCs in spinocerebel

22 oforms of PKC (PKC-betaI and PKC-alpha), and MARCKS-GFP, but only in Ca2+-containing solutions.

23 TRPC1 channels and MARCKS form signaling complexes with PI(4,5)P2 bound to

24 vel were increased with AKT1 inhibition, and MARCKS or LAMC2 knockdown abrogated migration and invasi

25 We determined that MARCKS and MARCKS-related protein specifically bind to LPS and that

26 ation and an intimate interaction of PSA and MARCKS at the cell surface was seen by confocal microsco

27 re in close contact, suggesting that PSA and MARCKS interact with each other at the plasma membrane f

28 Insertion of PSA and MARCKS-ED peptide into lipid bilayers from opposite side

29 rons confirm the interaction between PSA and MARCKS.

30 ifferences between properties of the PSD and MARCKS.

31 Both secretion and MARCKS phosphorylation were significantly enhanced by th

32 d PKC delta and enhanced mucin secretion and MARCKS phosphorylation.

33 F MPCs from control (CD44, cell surface; and MARCKS, intracellular).

34 functional role for the interaction between MARCKS and PSA in the developing and adult nervous syste

35 ivated protein kinase, and the actin-binding MARCKS protein--was blocked by preincubation with PEG-ca

36 ly downregulates proplatelet formation; both MARCKS and Arp2 were dephosphorylated in MKs making prop

37 results suggest that phosphorylation of both MARCKS and myosin II lead to disruption of the actin cor

38 BBS-mediated NT secretion was attenuated by MARCKS siRNA.

39 s TLC-mediated activation of PKC followed by MARCKS phosphorylation and consequent detachment of MARC

40 ng properties of Gag, the well-characterized MARCKS peptide, a series of fluorescent electrostatic se

41 tosol upon PMA treatment, further confirming MARCKS activation.

42 Conversely, MARCKS silencing had little or no effect on EC migration

43 g pathway molecules (ERK, JNK, CaMKII, CREB, MARCKS, Fyn, tau).

44 tion, whereas Sirtuin 2 (SIRT2) deacetylated MARCKS.

45 Phosphorylation dead MARCKS (PD-MARCKS) reversed maternal diabetes-induced ce

46 s transfected with phosphorylation-deficient MARCKS, TLC failed to increase MARCKS phosphorylation or

47 We demonstrate MARCKS silencing attenuates VSMC migration and arrests V

48 by Gay et al., suggests that effector domain MARCKS peptides could play a significant role in memory

49 In contrast, the cellular protein domain MARCKS and the PS sensor Evectin2 show preference for di

50 eptide corresponding to its effector domain, MARCKS(151-175), to sequester PIP2 in model membranes co

51 , or a peptide corresponding to this domain, MARCKS(151-175), sequesters several PI(4,5)P2 and that t

52 Endogenous MARCKS and green fluorescent protein-tagged wild-type MA

53 Knockdown of endogenous MARCKS using RNAi reduced spine density and size.

54 SA or PSA-NCAM and intracellularly expressed MARCKS-GFP are in close contact, suggesting that PSA and

55 CHO cells or hippocampal neurons expressing MARCKS as a fusion protein with green fluorescent protei

56 ed for membrane association is essential for MARCKS function in radial glia.

57 r cells were pharmacologically inhibited for MARCKS activity and subjected to functional bioassays.

58 tudies reveal a new regulatory mechanism for MARCKS acetylation and phosphorylation that disrupts neu

59 a and the Rho/ROK pathways are necessary for MARCKS activation.

60 that an atypical isoform was responsible for MARCKS phosphorylation.

61 Our findings establish a distinct role for MARCKS in the regulation of H(2)O(2)-induced permeabilit

62 These results suggest a key role for MARCKS PSD in cancer disease and provide a unique strate

63 These results indicate a crucial role for MARCKS, specifically its phosphorylated form, in potenti

64 ect role of MARCKS in proplatelet formation; MARCKS KO MKs displayed significantly decreased proplate

65 ts from MARCKS and release of PI(4,5)P2 from MARCKS; PI(4,5)P2 subsequently binds to TRPC1 subunits t

66 h causes dissociation of TRPC1 subunits from MARCKS and release of PI(4,5)P2 from MARCKS; PI(4,5)P2 s

67 We further demonstrated that higher MARCKS expression promotes growth and angiogenesis in vi

68 ever, behavioral consequences of hippocampal MARCKS peptide infusions have not been investigated.

69 d Phe residues play an essential role in how MARCKS-ED detects and binds to curved bilayers.

70 substrate and confirm previously identified MARCKS as a a bona fide Cdk5 substrate.

71 These data identify MARCKS as a pathogenic contributor to IH and indicate th

72 site domain sequence (MPS), to determine if MARCKS inhibition reduces pulmonary fibrosis through the

73 We aimed to determine if MARCKS PSD activity can serve as a therapeutic target an

74 MARCKS inhibited apoE secretion, implicating MARCKS as a downstream effector of PKC in apoE secretion

75 The critical role of PIP(2) in MARCKS responses was explored by examining the PIP(2)- a

76 TLC failed to increase MARCKS phosphorylation in HuH-NTCP cells transfected wit

77 ion-deficient MARCKS, TLC failed to increase MARCKS phosphorylation or decrease PM-MRP2.

78 TLC, but not cAMP, increased MARCKS phosphorylation in HuH-NTCP cells and hepatocytes

79 methacrylate (PMA), which markedly increased MARCKS phosphorylation while significantly inhibiting pr

80 , we show that high maternal glucose induced MARCKS acetylation at lysine 165 by the acetyltransferas

81 Intact MARCKS also does not bind as well to calmodulin as does

82 , yet paradoxically, we now find that intact MARCKS does not bind to actin.

83 e bilayer similar to that of the full-length MARCKS-ED peptide.

84 dating the function of one lncRNA, named lnc-MARCKS or ROCKI (Regulator of Cytokines and Inflammation

85 de comprising the effector domain of MARCKS (MARCKS-ED).

86 induced MRP2 retrieval involves PKC-mediated MARCKS phosphorylation.

87 s were markedly attenuated by siRNA-mediated MARCKS knockdown.

88 horylation of downstream signaling molecules MARCKS and PKCmu.

89 Moreover, MARCKS knockdown effectively abrogated N-WASP activation

90 singly, attenuation of MARCKS using the MPS (MARCKS phosphorylation site domain) peptide synergistica

91 ression of phosphorylation-deficient, mutant MARCKS greatly expands growth cone adhesion, and this is

92 Cells expressing this mutated MARCKS-ED SA4 show delayed onset of antigen-stimulated C

93 2.08 x 10(-7)), and rs7765004 at 6q21 (near MARCKS and HDAC2; HR, 1.38; 95% CI, 1.22 to 1.57; P = 7.

94 Nonphosphorylatable MARCKS caused spine elongation and increased the mobilit

95 However, myosin II, but not MARCKS, is required for the activity-dependent exocytosi

96 R4 signaling was enhanced by the ablation of MARCKS, which had no effect on stimulation by TLR2, TLR3

97 Here, we demonstrate that activation of MARCKS protein is important for PMA- and bombesin (BBS)-

98 ique strategy for inhibiting the activity of MARCKS PSD as a treatment for lung cancer.

99 o bind to actin and increase the affinity of MARCKS for calmodulin.

100 Surprisingly, attenuation of MARCKS using the MPS (MARCKS phosphorylation site domain

101 These results show the capacity of MARCKS-ED to regulate granule exocytosis in a PKC-depend

102 oth myristoylation of MARCKS and cleavage of MARCKS by calpain are shown to increase the availability

103 characterized by extensive colocalization of MARCKS and alpha3-integrin, resistance to eicosanoid-tri

104 H and examine the phenotypic consequences of MARCKS silencing by small interfering RNA (siRNA) transf

105 Our data suggest a major contribution of MARCKS to kidney cancer growth and provide an alternativ

106 Immunoblots confirm the degradation of MARCKS and fascin after preconditioning ischemia.

107 phosphorylation and consequent detachment of MARCKS from the membrane.

108 a peptide comprising the effector domain of MARCKS (MARCKS-ED).

109 e notion that PSA and the effector domain of MARCKS interact at and/or within the plane of the membra

110 By contrast, the myristoylation domain of MARCKS needed for membrane association is essential for

111 ng hypothesis is that the effector domain of MARCKS reversibly sequesters a significant fraction of t

112 S binding site within the effector domain of MARCKS was narrowed down to a heptapeptide that binds to

113 ctions between oppositely charged domains of MARCKS were responsible for long-range interactions with

114 A 25-mer peptide comprising the ED of MARCKS stimulates neuritogenesis of primary hippocampal

115 the cellular organelle protective effect of MARCKS.

116 ection technique to determine the effects of MARCKS silencing in human saphenous vein cultured ex viv

117 75) and short (amino acids 159-165) forms of MARCKS peptides could affect memory performance in the 1

118 e-sensing capabilities of seven fragments of MARCKS-ED.

119 However, the functionality of MARCKS and its related phosphorylation in lung cancer ma

120 A-NCAM) with MARCKS and co-immunostaining of MARCKS and PSA at the cell membrane of hippocampal neuro

121 hese cells, and direct peptide inhibition of MARCKS inhibited apoE secretion, implicating MARCKS as a

122 imilarly, small interfering RNA knockdown of MARCKS also increased LPS signaling, whereas overexpress

123 siRNA knockdown of MARCKS expression in these highly invasive lung cancer c

124 We found that siRNA-mediated knockdown of MARCKS in cultured endothelial cells abrogated directed

125 Following knockdown of MARCKS in RCC cells, the IC50 of the multikinase inhibit

126 siRNA-mediated knockdown of MARCKS or Rac1 attenuates receptor-mediated activation o

127 ) was blocked by siRNA-mediated knockdown of MARCKS, as determined using both biochemical assays and

128 This study demonstrated elevated levels of MARCKS and phospho-MARCKS in highly invasive lung cancer

129 We first observed that higher levels of MARCKS phosphorylation and the myofibroblast marker alph

130 nt with the MPS peptide suppressed levels of MARCKS phosphorylation in primary IPF fibroblasts.

131 Loss of MARCKS results in ectopic collection of mitotically acti

132 ply that post-translational modifications of MARCKS are necessary and sufficient to regulate actin-bi

133 h this hypothesis, chemical modifications of MARCKS that neutralize negatively charged residues outsi

134 Similarly, both myristoylation of MARCKS and cleavage of MARCKS by calpain are shown to in

135 sed LPS signaling, whereas overexpression of MARCKS inhibited LPS signaling.

136 r Ca(2+)-PKC and the PIP2-binding peptide of MARCKS modulate the level of free PIP2, which serves as

137 trate, surprisingly, that phosphorylation of MARCKS by PKC is not essential for the role of MARCKS in

138 is suggested PKC-mediated phosphorylation of MARCKS by TLC.

139 Phosphorylation of MARCKS causes its translocation from the membrane to the

140 Because phosphorylation of MARCKS modulates its actin crosslinking function, this l

141 duced mucin secretion and phosphorylation of MARCKS, whereas transfection of a wild-type construct in

142 did not lead to increased phosphorylation of MARCKS.

143 dose- and time-dependent phosphorylation of MARCKS.

144 I3K), and subsequently to phosphorylation of MARCKS.

145 lso substantially reduced in the presence of MARCKS-ED SA4, but store-operated Ca(2+) entry is not in

146 etion by airway epithelium via regulation of MARCKS phosphorylation.

147 We investigated the role of MARCKS (myristoylated, alanine-rich C-kinase substrate)

148 ll imaging approaches to explore the role of MARCKS in endothelial signal transduction pathways activ

149 The role of MARCKS in endothelial signaling responses is incompletel

150 Here, we further characterize the role of MARCKS in IH and examine the phenotypic consequences of

151 by C3 toxin, demonstrating that the role of MARCKS in NT secretion was regulated by PKC-delta downst

152 ockout (KO) mice to probe the direct role of MARCKS in proplatelet formation; MARCKS KO MKs displayed

153 RCKS by PKC is not essential for the role of MARCKS in radial glial cell development.

154 To examine the role of MARCKS in the PKC pathway, we treated MKs with polymetha

155 Because of the unusual primary sequence of MARCKS with an overall isoelectric point of 4.2 yet a ve

156 ments were taken from the central stretch of MARCKS-ED.

157 Genetic and pharmacologic suppression of MARCKS in high-grade RCC cell lines in vitro led to a de

158 ase of E-cadherin expression, suppression of MARCKS phosphorylation and AKT/Slug signalling pathway b

159 The membrane-associated targeting of MARCKS and the resultant polarized distribution of signa

160 Transcription of MARCKS is increased by stimulation with bacterial LPS.

161 ces the phosphorylation and translocation of MARCKS from the cell membrane to the cytosol.

162 on/metastasis and suggest a potential use of MARCKS-related peptides in the treatment of lung cancer

163 Calmodulin acting at, or upstream of, MARCKS is also required for TRPC1 channel opening throug

164 ovel pathway that is critically dependent on MARCKS, Rac1, and c-Abl.

165 angiotensin-II PIP(2) regulation depends on MARCKS and H(2)O(2).

166 uct did not affect either mucin secretion or MARCKS phosphorylation.

167 p-MARCKS also was enriched in the periphery of the actin c

168 Akt kinase activity, as well as downstream p-MARCKS and ribosomal p-S6.

169 e examined temporal and spatial changes in p-MARCKS localization during maturation of mouse oocytes a

170 ing revealed that the staining patterns of p-MARCKS and the active form of the atypical PKC zeta/lamb

171 KC isoforms did not increase the amount of p-MARCKS suggested that an atypical isoform was responsibl

172 Like pericentrin, p-MARCKS staining at the MI spindle poles was asymmetric.

173 nking function, this localization suggests p-MARCKS functions as part of the contractile apparatus du

174 however, the spindle poles had symmetrical p-MARCKS staining.

175 These results show that p-MARCKS is a novel centrosome component and also defines

176 maturation of mouse oocytes and found that p-MARCKS is a novel centrosome component based its co-loca

177 Phosphorylation dead MARCKS (PD-MARCKS) reversed maternal diabetes-induced cellular orga

178 ium exerted identical effects as those of PD-MARCKS.

179 the association of a 25-amino-acid peptide, MARCKS-ED, to membranes with and without spin labels.

180 in, we have employed a 25-mer novel peptide, MARCKS phosphorylation site domain sequence (MPS), to de

181 nditions, we demonstrate that cell permeable MARCKS effector domain (ED) peptides potently target all

182 trated elevated levels of MARCKS and phospho-MARCKS in highly invasive lung cancer cell lines and lun

183 63A) MARCKS, we showed that elevated phospho-MARCKS promoted cancer growth and erlotinib resistance.

184 We demonstrated that higher phospho-MARCKS levels were correlated with shorter overall survi

185 Interestingly, phospho-MARCKS acted in parallel with increased phosphatidylinos

186 The clinical relevance of phospho-MARCKS was first confirmed.

187 tasis in vivo, and reduced levels of phospho-MARCKS, phosphatidylinositol (3,4,5)-triphosphate, and A

188 tionality and molecular mechanism of phospho-MARCKS.

189 ted alanine-rich C kinase substrate (phospho-MARCKS) at the phosphorylation site domain (PSD) is cruc

190 e 3-kinase with MARCKS, but not with phospho-MARCKS.

191 Phosphorylated MARCKS dissociates from organelles, leading to mitochond

192 female-specific elevation of phosphorylated MARCKS levels after ED peptide treatment.

193 edema, this binding stabilizes the ENaC-PIP2-MARCKS complex, which is necessary for the open probabil

194 We investigated this hypothesized Ca(2+)-PKC-MARCKS-PIP2-PI3K-PIP3 amplification module and tested it

195 These findings 1) show that the Ca(2+)-PKC-MARCKS-PIP2-PI3K-PIP3 system functions as an activation

196 increased cytosolic pMARCKS and decreased PM-MARCKS in HuH-NTCP cells.

197 n endothelial cells, angiotensin-II-promoted MARCKS phosphorylation is abrogated by PEG-catalase, imp

198 ted alanine-rich C-kinase substrate protein (MARCKS), a prominent cellular substrate for PKC, modulat

199 ted proteins we characterized two proteins, :MARCKS (Myristoylated Alanine-Rich protein Kinase C subs

200 ubstrate phosphorylated at serine 46 (pSer46-MARCKS), and reveal an increase of neuronal necrosis dur

201 Moreover, expression of pseudophosphorylated MARCKS was, by itself, sufficient to induce spine loss a

202 ve hospitalization data suggests SAT1, PTEN, MARCKS and MAP3K3 might be not only state biomarkers but

203 y transfer from Bodipy-TMR-PIP2 to Texas Red MARCKS(151-175) adsorbed to large unilamellar vesicles.

204 odification from the promoter, thus reducing MARCKS transcription and subsequent Ca(2+) signaling and

205 published biomarkers for suicidality (SAT1, MARCKS and SKA2).

206 rted by Gay et al. that long, but not short, MARCKS peptides inhibit alpha7 nAChRs.

207 The shorter MARCKS peptide did not affect memory performance.

208 readily translated to the clinic to silence MARCKS in vein bypass grafts prior to implantation.

209 Silencing MARCKS expression dramatically reduces growth cone sprea

210 Similarly, MARCKS-ED tagged with monomeric red fluorescent protein

211 1 knockdown blocks angiotensin-II-stimulated MARCKS phosphorylation.

212 After LPS stimulation, MARCKS moved from the plasma membrane to FYVE-positive e

213 ntified the major protein kinase C substrate MARCKS (myristoylated alanine-rich C kinase substrate) a

214 ted alanine-rich protein kinase C substrate (MARCKS) correlated with modulation of PKC activity in th

215 ted alanine-rich protein kinase C substrate (MARCKS) is a cellular substrate for protein kinase C (PK

216 ted alanine-rich protein kinase C substrate (MARCKS) sequesters phosphoinositides at the inner leafle

217 ted alanine-rich protein kinase C substrate (MARCKS), and mitogen-activated protein kinase kinase kin

218 istoylated, alanine-rich C-kinase substrate (MARCKS) and fascin.

219 ristoylated alanine-rich C-kinase substrate (MARCKS) and LAMC2 protein level were increased with AKT1

220 ristoylated alanine-rich C kinase substrate (MARCKS) and release phosphatidylinositol-4,5-bisphosphat

221 ristoylated alanine-rich C kinase substrate (MARCKS) and these effects were abolished by ketanserin a

222 ristoylated alanine-rich C kinase substrate (MARCKS) and two newly considered feedback loops involvin

223 ristoylated alanine-rich C-kinase substrate (MARCKS) as a key mediator of the H(2)O(2)-induced permea

224 ristoylated alanine-rich C kinase substrate (MARCKS) as novel PSA binding partner.

225 ristoylated alanine-rich C-kinase substrate (MARCKS) bind to phosphatidylserine exposed on activated

226 ristoylated alanine-rich C-kinase substrate (MARCKS) could serve as a novel GBM therapeutic.

227 ristoylated alanine-rich C-kinase substrate (MARCKS) in this process.

228 ristoylated alanine-rich C kinase substrate (MARCKS) is a membrane-bound F-actin crosslinking protein

229 ristoylated alanine-rich C-kinase substrate (MARCKS) is an intracellular receptor for polysialic acid

230 ristoylated alanine-rich C kinase substrate (MARCKS) is an intrinsically unfolded protein with a cons

231 ristoylated alanine-rich C kinase substrate (MARCKS) is an unfolded protein that contains well charac

232 ristoylated alanine-rich C kinase substrate (MARCKS) peptide comprising the phosphorylation site or e

233 ristoylated alanine-rich C kinase substrate (MARCKS) protein coordinates activation of TRPC1 channels

234 ristoylated alanine-rich C kinase substrate (MARCKS) protein in these cells.

235 ristoylated alanine-rich C kinase substrate (MARCKS) which interacts with PSA within the plane of the

236 ristoylated alanine-rich C kinase substrate (MARCKS), a key protein kinase C (PKC) substrate, to be u

237 ristoylated Alanine-Rich C Kinase Substrate (MARCKS), a substrate of protein kinase C, is a key regul

238 ristoylated alanine-rich C-kinase substrate (MARCKS), as a potential target molecule for IPF.

239 ristoylated alanine-rich C kinase substrate (MARCKS), or a peptide corresponding to this domain, MARC

240 ristoylated alanine-rich C-kinase substrate (MARCKS), which was upregulated 3.4- and 5.7-fold in prop

241 istoylated, alanine-rich C-kinase substrate (MARCKS).

242 yristolated alanine-rich C-kinase substrate (MARCKS).

243 ristoylated alanine-rich C-kinase substrate (MARCKS-ED) has been demonstrated to have curvature-sensi

244 Our data suggest MARCKS as a druggable target in pulmonary fibrosis and a

245 Tackling MARCKS-PIP3 circuit attenuates fibroblast activation and

246 s necessary for growth cone turning and that MARCKS, while at the membrane, colocalizes with alpha3-i

247 We conclude that MARCKS is involved in regulating growth cone adhesion as

248 undant evidence supports the conclusion that MARCKS is an important protein in regulating actin dynam

249 These findings demonstrate that MARCKS contributes to the negative regulation of the cel

250 Our data demonstrate that MARCKS phosphorylation under elevated cell firing is req

251 We determined that MARCKS and MARCKS-related protein specifically bind to L

252 We find that MARCKS-ED dissociation is prevented by mutation of four

253 les from 56 patients with RCC, we found that MARCKS expression and its phosphorylation are increased

254 We hypothesized that MARCKS phosphorylation promotes Arp2/3 phosphorylation,

255 These results indicate that MARCKS ED peptide therapeutics may overcome traditional

256 We propose that MARCKS acts as a "molecular switch," binding to and regu

257 ng and hydrodynamic approaches revealed that MARCKS is targeted to plasmalemmal caveolae and undergoe

258 These novel findings show that MARCKS coordinates native TRPC1 channel activation in VS

259 Here we show that MARCKS is expressed in intact arterial preparations, wit

260 Taken together, these studies show that MARCKS plays a key role in insulin-dependent endothelial

261 g proplatelet formation 84%, suggesting that MARCKS phosphorylation reduces proplatelet formation.

262 The MARCKS peptides antagonize the binding of factor Xa to p

263 The MARCKS protein (myristoylated alanine-rich C kinase subs

264 The MARCKS-ED peptide abolished PSA-induced enhancement of n

265 ) to form a ribonucleoprotein complex at the MARCKS promoter.

266 Consistent with pelleting data, the MARCKS peptide showed preference for the Ld domain.

267 In whole blood under flow, the MARCKS peptides colocalize with, and inhibit fibrin cros

268 e off state of the amplification module, the MARCKS peptide sequesters PIP2 and thereby inhibits PI3K

269 lly bind to LPS and that the addition of the MARCKS effector peptide inhibited LPS-induced production

270 y assays, meanwhile, reveal that five of the MARCKS fragments possess the ability to sense membrane c

271 on state, Ca(2+)-PKC phosphorylation of the MARCKS peptide reverses the PIP2 sequestration, thereby

272 We also found that the effect of the MARCKS(151-175) peptide was dose-dependent, with a robus

273 Research of the MARCKS-ED has further revealed that its Lys and Phe resi

274 reatment with a 25-mer peptide targeting the MARCKS PSD motif (MPS peptide), we were able to suppress

275 In vivo, we find that the MARCKS peptides circulate to remote injuries and bind to

276 y, treatment with a peptide identical to the MARCKS N-terminus sequence (the MANS peptide) impaired c

277 inal targeting region have similarity to the MARCKS proteins and were found to control AKAP12 localiz

278 ted and unsaturated acyl chains, whereas the MARCKS peptide and Evectin2 preferentially bound to memb

279 c contributor to IH and indicate therapeutic MARCKS silencing could selectively suppress the "atherog

280 Thus, MARCKS is a key factor in the maintenance of dendritic s

281 he N terminus alters how calmodulin binds to MARCKS, implying that, despite its unfolded state, the d

282 signaling complexes with PI(4,5)P2 bound to MARCKS; in this configuration TRPC1 channels are closed.

283 a that is triggered by H(2)O(2) and leads to MARCKS phosphorylation.

284 Small interfering RNA (siRNA) to MARCKS significantly inhibited, whereas overexpression o

285 the free PSD binds with site specificity to MARCKS, suggesting that long-range intramolecular intera

286 ling pathway but not the expression of total MARCKS.

287 spread, whereas overexpression of wild-type MARCKS inhibits growth cone collapse triggered by PKC ac

288 hibited, whereas overexpression of wild-type MARCKS significantly increased PMA-mediated NT secretion

289 d green fluorescent protein-tagged wild-type MARCKS were translocated from membrane to cytosol upon P

290 ce spectra of spin-labeled PIP2 as unlabeled MARCKS(151-175) adsorbs to vesicles.

291 in large unilamellar vesicles when unlabeled MARCKS(151-175) binds to vesicles.

292 e inner leaflet of the plasma membrane until MARCKS dissociates after phosphorylation by activated PK

293 Finally, we used MARCKS knockout (KO) mice to probe the direct role of MA

294 Compound 8 interfered with MARCKS phosphorylation and TPA-induced translocation of

295 nteraction of phosphoinositide 3-kinase with MARCKS, but not with phospho-MARCKS.

296 anging) and reference (constant) memory with MARCKS(151-175) only.

297 eural cell adhesion molecule (PSA-NCAM) with MARCKS and co-immunostaining of MARCKS and PSA at the ce

298 primary hippocampal neurons transfected with MARCKS.

299 ong-range intramolecular interactions within MARCKS are also possible.

300 sponsible for long-range interactions within MARCKS that sterically influence binding events at the P